ID   IMND1_VIBCR             Reviewed;         399 AA.
AC   C9NUM5;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=D-galactonate dehydratase family member VIC002985;
GN   ORFNames=VIC_002985;
OS   Vibrio coralliilyticus (strain ATCC BAA-450 / DSM 19607 / CCUG 48437 / LMG
OS   20984 / YB1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=675814;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-450 / DSM 19607 / CCUG 48437 / LMG 20984 / YB1;
RX   PubMed=22158392; DOI=10.1038/ismej.2011.154;
RA   Kimes N.E., Grim C.J., Johnson W.R., Hasan N.A., Tall B.D., Kothary M.H.,
RA   Kiss H., Munk A.C., Tapia R., Green L., Detter C., Bruce D.C.,
RA   Brettin T.S., Colwell R.R., Morris P.J.;
RT   "Temperature regulation of virulence factors in the pathogen Vibrio
RT   coralliilyticus.";
RL   ISME J. 6:835-846(2012).
RN   [2]
RP   FUNCTION, AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
RC   STRAIN=ATCC BAA-450 / DSM 19607 / CCUG 48437 / LMG 20984 / YB1;
RX   PubMed=24697546; DOI=10.1021/bi500264p;
RA   Wichelecki D.J., Balthazor B.M., Chau A.C., Vetting M.W., Fedorov A.A.,
RA   Fedorov E.V., Lukk T., Patskovsky Y.V., Stead M.B., Hillerich B.S.,
RA   Seidel R.D., Almo S.C., Gerlt J.A.;
RT   "Discovery of function in the enolase superfamily: D-mannonate and D-
RT   gluconate dehydratases in the D-mannonate dehydratase subgroup.";
RL   Biochemistry 53:2722-2731(2014).
CC   -!- FUNCTION: Has no detectable activity with D-mannonate and with a panel
CC       of 70 other acid sugars (in vitro), in spite of the conservation of the
CC       residues that are expected to be important for catalytic activity and
CC       cofactor binding. May have evolved a divergent function.
CC       {ECO:0000269|PubMed:24697546}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GalD subfamily. {ECO:0000305}.
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DR   EMBL; ACZN01000017; EEX31886.1; -; Genomic_DNA.
DR   RefSeq; WP_006960953.1; NZ_ACZN01000017.1.
DR   AlphaFoldDB; C9NUM5; -.
DR   SMR; C9NUM5; -.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 1.
DR   InterPro; IPR034589; D-mannonate_dehydratase-like.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR034593; Mandelate_racemase_DgoD-like.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48080; PTHR48080; 1.
DR   PANTHER; PTHR48080:SF6; PTHR48080:SF6; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDG00033; mannonate_dehydratase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
DR   PROSITE; PS00908; MR_MLE_1; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding.
FT   CHAIN           1..399
FT                   /note="D-galactonate dehydratase family member VIC002985"
FT                   /id="PRO_0000429918"
FT   BINDING         205
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         334
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   399 AA;  45264 MW;  B26EE1E6E153D578 CRC64;
     MNTTIITDVE CIITKPDRHN LITVIVHTNN GTVGYGCATF QQRPLAVKTM VDEYLKPLLI
     GKDANNIEDL WQMMMVNAYW RNGPVINNAV SGVDMALWDI KAKQAKMPLH QLFGGKSRDA
     IAVYTHATSD SMEGLYESID NYLKQGYRHI RCQLGFYGGV PEALHTTQNP TVGSYYDQDQ
     YVENTVTMFK LLREKYGNQF HILHDVHERL FPNQAVQFAK DVEKYKPYFI EDILPPNQTE
     WLDNIRSQTS VSLGLGELFN NPEEWKSLII NRRIDFIRCH VSQIGGITPA LKLGHLCQTF
     GVRIAWHCPP DMTPIGAAVN THLNVHLHNA AIQEHVEYKE NTRKVFPGAS EPKNGYLYAS
     ELSGIGVEID TEVAADFPVT YRPHEWTQSR LPDGTIHTP